1:2 complex of human growth hormone with its soluble binding protein. Determined by X-ray diffraction at 2.5 Å resolution. Released 19 Nov 1997.
Explore 1HWG in 3D Show helices and sheets RCSB PDB PDBe
1HWG contains 18 α-helices and 36 β-strands across 3 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-35 | 30 | |
| α-helix | 38-46 | 9 | |
| α-helix | 54-57 | 4 | |
| α-helix | 64-67 | 4 | |
| α-helix | 72-87 | 16 | |
| α-helix | 89-93 | 5 | |
| α-helix | 94-98 | 5 | |
| α-helix | 107-127 | 21 | |
| α-helix | 143-146 | 4 | |
| α-helix | 155-184 | 30 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 35-39 | 5 | 1 |
| β-strand | 40 | 1 | 2 |
| β-strand | 46-50 | 5 | 1 |
| β-strand | 64-70 | 7 | 3 |
| β-strand | 81-82 | 2 | 3 |
| β-strand | 93-96 | 4 | 1 |
| α-helix | 98-100 | 3 | |
| β-strand | 106-113 | 8 | 3 |
| β-strand | 116-124 | 9 | 3 |
| α-helix | 125-128 | 4 | |
| β-strand | 129 | 1 | 2 |
| β-strand | 135-144 | 10 | 4 |
| β-strand | 150-158 | 9 | 4 |
| β-strand | 172-180 | 9 | 5 |
| β-strand | 187-188 | 2 | 5 |
| β-strand | 192 | 1 | 5 |
| β-strand | 196-203 | 8 | 4 |
| β-strand | 207-216 | 10 | 5 |
| α-helix | 227-228 | 2 | |
| β-strand | 229-232 | 4 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 35-39 | 5 | 6 |
| β-strand | 40 | 1 | 7 |
| β-strand | 46-50 | 5 | 6 |
| β-strand | 64-69 | 6 | 8 |
| β-strand | 81-82 | 2 | 8 |
| β-strand | 93-96 | 4 | 6 |
| β-strand | 107-113 | 7 | 8 |
| β-strand | 116-123 | 8 | 8 |
| α-helix | 125-128 | 4 | |
| β-strand | 129 | 1 | 7 |
| α-helix | 131-134 | 4 | |
| β-strand | 135-144 | 10 | 9 |
| β-strand | 150-158 | 9 | 9 |
| α-helix | 161-164 | 4 | |
| β-strand | 173-180 | 8 | 10 |
| β-strand | 187-188 | 2 | 10 |
| α-helix | 189-191 | 3 | |
| β-strand | 192 | 1 | 10 |
| β-strand | 196-203 | 8 | 9 |
| β-strand | 207-215 | 9 | 10 |
| β-strand | 216 | 1 | 11 |
| β-strand | 219 | 1 | 11 |
| β-strand | 229-232 | 4 | 10 |
| α-helix | 233-236 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Growth hormone | A | protein | 191 | Homo sapiens | P01241 (AlphaFold model) |
| Growth hormone binding protein | B, C | protein | 237 | Homo sapiens | P10912 (AlphaFold model) |
>1HWG_1 GROWTH HORMONE (chains A) FPTIPLSRLFDNAMLRAHRLHQLAFDTYQEFEEAYIPKEQKYSFLQNPQTSLCFSESIPT PSNREETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLLKDLEEG IQTLMGRLEDGSPRTGQIFKQTYSKFDTNSHNDDALLKNYGLLYCFRKDMDKVETFLRIV QCRSVEGSCGF
>1HWG_2 GROWTH HORMONE BINDING PROTEIN (chains B, C) FSGSEATAAILSRAPWSLQSVNPGLKTNSSKEPKFTKCRSPERETFSCHWTDEVHHGTKN LGPIQLFYTRRNTQEWTQEWKECPDYVSAGENSCYFNSSFTSIWIPYCIKLTSNGGTVDE KCFSVDEIVQPDPPIALNWTLLNVSLTGIHADIQVRWEAPRNADIQKGWMVLEYELQYKE VNETKWKMMDPILTTSVPVYSLKVDKEYEVRVRSKQRNSGNYGEFSEVLYVTLPQMS
Crystal structure of an antagonist mutant of human growth hormone, G120R, in complex with its receptor at 2.9 A resolution. Sundstrom, M., Lundqvist, T., Rodin, J. et al. J Biol Chem (1996) 271:32197-32203. DOI 10.1074/jbc.271.50.32197 · PubMed
Other PDB entries of the same protein (UniProt P01241 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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